Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
about
DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 bindingAurora B and 14-3-3 coordinately regulate clustering of centralspindlin during cytokinesisDifferential 14-3-3 affinity capture reveals new downstream targets of phosphatidylinositol 3-kinase signalingProteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosisStratifin (14-3-3 σ) limits plakophilin-3 exchange with the desmosomal plaque14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cellsThe role of prostate tumor overexpressed 1 in cancer progressionThree-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranesPhospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage responseThe interactome of a PTB domain-containing adapter protein, Odin, revealed by SILACProtein kinase D1 mediates anchorage-dependent and -independent growth of tumor cells via the zinc finger transcription factor Snail1An inflammatory bowel disease-risk variant in INAVA decreases pattern recognition receptor-induced outcomes14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesisThe first small-molecule inhibitor of 14-3-3s: modulating the master regulator.Role of 14-3-3σ in poor prognosis and in radiation and drug resistance of human pancreatic cancers.A novel role for 14-3-3sigma in regulating epithelial cell polarity.14-3-3ε boosts bleomycin-induced DNA damage response by inhibiting the drug-resistant activity of MVPProteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana.Keratin 23, a novel DPC4/Smad4 target gene which binds 14-3-3ε.Expression of 14-3-3 protein isoforms in mouse oocytes, eggs and ovarian follicular developmentEffects of partner proteins on BCA2 RING ligase activity.14-3-3ε mediates the cell fate decision-making pathways in response of hepatocellular carcinoma to Bleomycin-induced DNA damage.A robust protocol to map binding sites of the 14-3-3 interactome: Cdc25C requires phosphorylation of both S216 and S263 to bind 14-3-3A role of TGFß1 dependent 14-3-3σ phosphorylation at Ser69 and Ser74 in the regulation of gene transcription, stemness and radioresistanceAnalysis and prediction of pathways in HeLa cells by integrating biological levels of organization with systems-biology approachesInteraction of 14-3-3σ with KCMF1 suppresses the proliferation and colony formation of human colon cancer stem cells.14-3-3σ and p63 play opposing roles in epidermal tumorigenesis.Structure-Function Analysis of PPP1R3D, a Protein Phosphatase 1 Targeting Subunit, Reveals a Binding Motif for 14-3-3 Proteins which Regulates its Glycogenic Properties14-3-3σ confers cisplatin resistance in esophageal squamous cell carcinoma cells via regulating DNA repair molecules.The Human Papillomavirus E6 PDZ Binding Motif: From Life Cycle to Malignancy.Osteogenic differentiation of human placenta-derived mesenchymal stem cells (PMSCs) on electrospun nanofiber meshes.Verification of single-peptide protein identifications by the application of complementary database search algorithms.HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class I (MHC-I) down-regulation: analysis using short interfering RNA and knock-out mice.Expression of 14-3-3sigma, p16 and p53 proteins in anal squamous intraepithelial neoplasm and squamous cell carcinomaProtein partners of deubiquitinating enzymes.Determinants of 14-3-3σ protein dimerization and function in drug and radiation resistance.14-3-3 Protein regulates cell adhesion in the seminiferous epithelium of rat testes.14-3-3σ attenuates RhoGDI2-induced cisplatin resistance through activation of Erk and p38 in gastric cancer cells.14-3-3sigma, the double-edged sword of human cancersDeletion of 14-3-3σ sensitizes mice to DMBA/TPA-induced papillomatosis.
P2860
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P248
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P2860
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
description
2005 nî lūn-bûn
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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
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2005年の論文
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2005年論文
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2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
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2005年论文
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name
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@ast
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en-gb
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@nl
type
label
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@ast
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en-gb
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@nl
prefLabel
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@ast
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en-gb
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@nl
P2093
P2860
P3181
P1476
Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
@en
P2093
Anne Benzinger
Heike B Koch
Heiko Hermeking
John R Yates
Nemone Muster
P2860
P304
P3181
P356
10.1074/MCP.M500021-MCP200
P407
P577
2005-06-01T00:00:00Z